GPCRDB: Swiss-Prot entry

ID   PRIO_CAMDR     STANDARD;      PRT;   255 AA.
AC   P79141;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Major prion protein precursor (PrP).
GN   Name=PRNP; Synonyms=PRP;
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Cetartiodactyla; Tylopoda; Camelidae; Camelus. 
OX   NCBI_TaxID=9838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=98019099; PubMed=9358067 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0378-1119(97)00382-X;
RA   Kaluz S., Kaluzova M., Flint A.P.F.;
RT   "Sequencing analysis of prion genes from red deer and camel.";
RL   Gene 199:283-286(1997).
CC   -!- FUNCTION: The function of PrP is not known. PrP is encoded in the
CC       host genome and is expressed both in normal and infected cells.
CC   -!- SUBUNIT: PrP has a tendency to aggregate yielding polymers called
CC       "rods".
CC   -!- SUBCELLULAR LOCATION: Attached to the membrane by a GPI-anchor.
CC   -!- DISEASE: PrP is found in high quantity in the brain of humans and
CC       animals infected with the degenerative neurological diseases kuru,
CC       Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome
CC       (GSS), scrapie, bovine spongiform encephalopathy (BSE),
CC       transmissible mink encephalopathy (TME), etc.
CC   -!- SIMILARITY: Belongs to the prion family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; Y09760; CAA70901.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P23907; 1G04. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   InterPro; IPR000817; Prion.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00377; Prion; 1.
DR   Pfam; PF03991; Prion_octapep; 5.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00341; PRION.
DR   PROSITE; PS00291; PRION_1; 1.
DR   PROSITE; PS00706; PRION_2; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P79141.
DR   ProtoNet; P79141.
DR   ProtoMap; P79141.
DR   PRESAGE; P79141.
DR   DIP; P79141.
DR   ModBase; P79141.
DR   SMR; P79141.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Prion; Repeat;
KW   Signal.
FT   SIGNAL        1     24       By similarity.
FT   CHAIN        25    233       Major prion protein.
FT   PROPEP      234    255       Removed in mature form (Potential).
FT   DOMAIN       54     94       5 X 8 AA tandem repeats of P-H-G-G-G-W-G-
FT                                Q.
FT   REPEAT       54     62       1.
FT   REPEAT       63     70       2.
FT   REPEAT       71     78       3.
FT   REPEAT       79     86       4.
FT   REPEAT       87     94       5.
FT   DISULFID    182    217       By similarity.
FT   LIPID       233    233       GPI-anchor amidated alanine (Potential).
FT   CARBOHYD    184    184       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   255 AA;  27595 MW;  FABB2DBFA333E494 CRC64;
     MVKSHMGSWI LVLFVVTWSD VGLCKKRPKP GGGWNTGGSR YPGQGSPGGN RYPPQGGGGW
     GQPHGGGWGQ PHGGGWGQPH GGGWGQPHGG GWGQGGGAHG QWNKPSKPKT SMKHVAGAAA
     AGAVVGGLGG YMLGSAMSRP LIHFGNDYED RYYRENMYRY PNQVYYKPVD QYSNQNSFVH
     DCVNITVKQH TVTTTTKGEN FTETDVKMME RVVEQMCITQ YQREYQASYG RGASVIFSSP
     PVILLISFLI FLIVG
//